EC Number | Cloned (Comment) | Organism |
---|---|---|
3.2.1.15 | homologously overexpressed | Aspergillus niger |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.2.1.15 | 36000 | - |
MALDI-TOF MS, PGA lacking N-glycan modification | Aspergillus niger |
3.2.1.15 | 36200 | - |
MALDI-TOF MS, deglycosylated PGA | Aspergillus niger |
3.2.1.15 | 37230 | - |
MALDI-TOF MS, recombinant PGA | Aspergillus niger |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.15 | Aspergillus niger | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.2.1.15 | - |
Aspergillus niger |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.15 | additional information | N- and O-glycosylated. N-linked glycosylation at Asn214, but O-linked glycosylation at any serine or threonine residue. N-linked glycan attached at PGA Asn214 contains a high-mannose structure of GlcNAc2Man4-9 | Aspergillus niger | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.2.1.15 | endo-polygalacturonase A | - |
Aspergillus niger |
3.2.1.15 | PGA | - |
Aspergillus niger |